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==STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION==
==STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION==
<StructureSection load='1svr' size='340' side='right'caption='[[1svr]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1svr' size='340' side='right'caption='[[1svr]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1svr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SVR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1svr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SVR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1svq|1svq]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1svr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svr OCA], [https://pdbe.org/1svr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svr RCSB], [https://www.ebi.ac.uk/pdbsum/1svr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svr ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1svr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svr OCA], [https://pdbe.org/1svr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svr RCSB], [https://www.ebi.ac.uk/pdbsum/1svr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SEVE_DICDI SEVE_DICDI]] Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner.  
[https://www.uniprot.org/uniprot/SEVE_DICDI SEVE_DICDI] Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca(2+) dependent manner.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svr ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svr ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of domain 2 of severin in aqueous solution was determined by nuclear magnetic resonance spectroscopy. Severin is a Ca(2+)-activated actin-binding protein that servers F-actin, nucleates actin assembly, and caps the fast-growing ends of actin filaments. The 114-residue domain consists of a central five-stranded beta-sheet, sandwiched between a parallel four-turn alpha-helix and, on the other face, a roughly perpendicular two-turn alpha-helix. There are two distinct binding sites for Ca2+ located near the N and C termini of the long helix. Conserved residues of the gelsolin-severin family contribute to the apolar core of domain 2 of severin, so that the overall fold of the protein is similar to those of segment 1 of gelsolin and profilins. Together with biochemical experiments, this structure helps to explain how severin interacts with actin.
Structure of severin domain 2 in solution.,Schnuchel A, Wiltscheck R, Eichinger L, Schleicher M, Holak TA J Mol Biol. 1995 Mar 17;247(1):21-7. PMID:7897658<ref>PMID:7897658</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1svr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Severin|Severin]]
*[[Severin|Severin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 11735]]
[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Holak, T A]]
[[Category: Holak TA]]
[[Category: Schnuchel, A]]
[[Category: Schnuchel A]]
[[Category: Actin-binding]]

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